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Protein

FK506-binding protein 4

Gene

FPR4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PPIase that acts as a histone chaperone (PubMed:14981505, PubMed:16846601). Histone proline isomerase that increases the rate of cis-trans isomerization at 'Pro-17' (H3P16), 'Pro-31' (H3P30) and 'Pro-39 (H3P38) on the histone H3 N-terminal tail (PubMed:16959570, PubMed:23888048). H3P16 and H3P30 are the major proline targets with little activity shown against H3P38 (PubMed:23888048). H3P38 isomerization influences SET2-mediated H3K36 methylation thereby regulating gene expression (PubMed:16959570).4 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).2 Publications

GO - Molecular functioni

  • macrolide binding Source: SGD
  • peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

  • histone peptidyl-prolyl isomerization Source: SGD
  • negative regulation of histone H3-K36 methylation Source: SGD
  • nucleosome assembly Source: SGD
  • protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YLR449W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FK506-binding protein 41 Publication (EC:5.2.1.82 Publications)
Alternative name(s):
Histone proline isomerase1 Publication
Peptidyl-prolyl cis-trans isomerase
Short name:
PPIase
Rotamase
Gene namesi
Name:FPR41 Publication
Ordered Locus Names:YLR449WImported
ORF Names:L9324.3
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR449W.
SGDiS000004441. FPR4.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392FK506-binding protein 4PRO_0000075314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei82 – 821PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06205.
PeptideAtlasiQ06205.
PRIDEiQ06205.

PTM databases

iPTMnetiQ06205.

Interactioni

Subunit structurei

Binds to histones H3 and H4 (PubMed:16959570). Interacts with NOP53.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HHF2P023095EBI-6956,EBI-8113
HHT2P618305EBI-6956,EBI-8098
LOC1P435863EBI-6956,EBI-22906

Protein-protein interaction databases

BioGridi31707. 86 interactions.
DIPiDIP-909N.
IntActiQ06205. 69 interactions.
MINTiMINT-8285380.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi282 – 2854Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi308 – 31710Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi339 – 3413Combined sources
Helixi343 – 3486Combined sources
Beta strandi357 – 3626Combined sources
Helixi364 – 3663Combined sources
Turni367 – 3704Combined sources
Beta strandi382 – 39211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BF8NMR-A280-392[»]
ProteinModelPortaliQ06205.
SMRiQ06205. Positions 240-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini306 – 39287PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 1999Poly-Glu

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000064286.
HOGENOMiHOG000216214.
InParanoidiQ06205.
KOiK14826.
OMAiQAIDITI.
OrthoDBiEOG77WWQ3.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDMLPLATY SLNVEPYSPT PALNFKIPVT IRITMAAIDP EPFDDDKKPS
60 70 80 90 100
TLRIIKRNPE LTRGEYYNQD NNDGLEEDES ESEQEADVPK RSVKSKKGKA
110 120 130 140 150
VEQSESEDSE DENEIDDEFE ECVLLTLSPK GQYQQALDIT IAPEEDVQFV
160 170 180 190 200
VTGSYTISLT GNYVKHPFDN SSDSDEDEED YYSDEESSNG EEEEEEEEED
210 220 230 240 250
DEELSSGDDD LDDLVDASDI ESRLDELVKK DEKKKNNKKD SKRKHEEDEE
260 270 280 290 300
ESAKPAEKKQ TTKKDKKAEK VKDSEESKPK PKTKLLEGGI IIEDRVTGKG
310 320 330 340 350
PHAKKGTRVG MRYVGKLKNG KVFDKNTKGK PFVFKLGQGE VIKGWDIGVA
360 370 380 390
GMAVGGERRI VIPAPYAYGK QALPGIPANS ELTFDVKLVS MK
Length:392
Mass (Da):43,903
Last modified:November 1, 1996 - v1
Checksum:iCF90C6714F04572E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22382 Genomic DNA. Translation: AAB67528.1.
BK006945 Genomic DNA. Translation: DAA09749.1.
PIRiS55971.
RefSeqiNP_013554.3. NM_001182337.3.

Genome annotation databases

EnsemblFungiiYLR449W; YLR449W; YLR449W.
GeneIDi851170.
KEGGisce:YLR449W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22382 Genomic DNA. Translation: AAB67528.1.
BK006945 Genomic DNA. Translation: DAA09749.1.
PIRiS55971.
RefSeqiNP_013554.3. NM_001182337.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BF8NMR-A280-392[»]
ProteinModelPortaliQ06205.
SMRiQ06205. Positions 240-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31707. 86 interactions.
DIPiDIP-909N.
IntActiQ06205. 69 interactions.
MINTiMINT-8285380.

PTM databases

iPTMnetiQ06205.

Proteomic databases

MaxQBiQ06205.
PeptideAtlasiQ06205.
PRIDEiQ06205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR449W; YLR449W; YLR449W.
GeneIDi851170.
KEGGisce:YLR449W.

Organism-specific databases

EuPathDBiFungiDB:YLR449W.
SGDiS000004441. FPR4.

Phylogenomic databases

GeneTreeiENSGT00530000064286.
HOGENOMiHOG000216214.
InParanoidiQ06205.
KOiK14826.
OMAiQAIDITI.
OrthoDBiEOG77WWQ3.

Enzyme and pathway databases

BioCyciYEAST:YLR449W-MONOMER.

Miscellaneous databases

NextBioi967978.
PROiQ06205.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae."
    Dolinski K., Muir S., Cardenas M., Heitman J.
    Proc. Natl. Acad. Sci. U.S.A. 94:13093-13098(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing."
    Kuzuhara T., Horikoshi M.
    Nat. Struct. Mol. Biol. 11:275-283(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein."
    Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D.
    Biochem. J. 388:819-826(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOP53, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Proline isomerization of histone H3 regulates lysine methylation and gene expression."
    Nelson C.J., Santos-Rosa H., Kouzarides T.
    Cell 126:905-916(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HISTONE H3 AND H4.
  8. "The FK506-binding protein, Fpr4, is an acidic histone chaperone."
    Xiao H., Jackson V., Lei M.
    FEBS Lett. 580:4357-4364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization."
    Monneau Y.R., Soufari H., Nelson C.J., Mackereth C.D.
    J. Biol. Chem. 288:25826-25837(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 280-392, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiFKBP4_YEAST
AccessioniPrimary (citable) accession number: Q06205
Secondary accession number(s): D6VZ83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 14100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.